PDBsum entry 1vhn

Structural genomics, unknown function

PDB id

1vhn

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Contents

			Protein chain

					305 a.a. *

			Ligands

					SO4 ×3


					FMN

			Waters ×315

* Residue conservation analysis

PDB id:

1vhn

Links
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Name:

Structural genomics, unknown function

Title:

Crystal structure of a putative flavin oxidoreductase with flavin

Structure:

Putative flavin oxidoreductase. Chain: a. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: yacf. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.59Å

R-factor:

0.189

R-free:

0.227

Authors:

Structural Genomix

Key ref:

F.Park et al. (2004). The 1.59 A resolution crystal structure of TM0096, a flavin mononucleotide binding protein from Thermotoga maritima. Proteins, 55, 772-774. PubMed id: 15103641 DOI: 10.1002/prot.20086

Date:

01-Dec-03

Release date:

30-Dec-03

PROCHECK

	Headers

	References

Protein chain

Q9WXV1 (Q9WXV1_THEMA) - tRNA-dihydrouridine synthase from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: Struc:					306 a.a. 305 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.1.3.1.- - ?????

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1002/prot.20086	Proteins 55:772-774 (2004)
PubMed id: 15103641

The 1.59 A resolution crystal structure of TM0096, a flavin mononucleotide binding protein from Thermotoga maritima.
F.Park, K.Gajiwala, B.Noland, L.Wu, D.He, J.Molinari, K.Loomis, B.Pagarigan, P.Kearins, J.Christopher, T.Peat, J.Badger, J.Hendle, J.Lin, S.Buchanan.

ABSTRACT

No abstract given.

Selected figure(s)



	Figure 1. Figure 1. A: SPOCK[17] ribbon diagram of TM0096 protein with FMN cofactor and three sulfate ions. -strands and -helices are shown in cyan and orange, respectively. B: Absorbance spectrum of the oxidized FMN cofactor in the TM0096 protein. inset: Expanded view of same spectrum showing relative absorbance between the protein (A[280]) and the cofactor (A[450]). C: Putative catalytic residues and substrate binding site residues are rendered as ball-and-stick figures in yellow and grey, respectively. The FMN moiety is rendered as white ball-and-stick.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19139092

L.W.Rider, M.B.Ottosen, S.G.Gattis, and B.A.Palfey (2009).
Mechanism of Dihydrouridine Synthase 2 from Yeast and the Importance of Modifications for Efficient tRNA Reduction.

J Biol Chem, 284, 10324-10333.

16021622

J.Badger, J.M.Sauder, J.M.Adams, S.Antonysamy, K.Bain, M.G.Bergseid, S.G.Buchanan, M.D.Buchanan, Y.Batiyenko, J.A.Christopher, S.Emtage, A.Eroshkina, I.Feil, E.B.Furlong, K.S.Gajiwala, X.Gao, D.He, J.Hendle, A.Huber, K.Hoda, P.Kearins, C.Kissinger, B.Laubert, H.A.Lewis, J.Lin, K.Loomis, D.Lorimer, G.Louie, M.Maletic, C.D.Marsh, I.Miller, J.Molinari, H.J.Muller-Dieckmann, J.M.Newman, B.W.Noland, B.Pagarigan, F.Park, T.S.Peat, K.W.Post, S.Radojicic, A.Ramos, R.Romero, M.E.Rutter, W.E.Sanderson, K.D.Schwinn, J.Tresser, J.Winhoven, T.A.Wright, L.Wu, J.Xu, and T.J.Harris (2005).
Structural analysis of a set of proteins resulting from a bacterial genomics project.

Proteins, 60, 787-796.

PDB codes:

1o60 1o61 1o62 1o63 1o64 1o65 1o66 1o67 1o68 1o69 1o6b 1o6c 1o6d 1vgt 1vgu 1vgv 1vgw 1vgx 1vgy 1vgz 1vh0 1vh1 1vh2 1vh3 1vh4 1vh5 1vh6 1vh7 1vh8 1vh9 1vha 1vhc 1vhd 1vhe 1vhf 1vhg 1vhj 1vhk 1vhl 1vhm 1vho 1vhq 1vhs 1vht 1vhu 1vhv 1vhw 1vhx 1vhy 1vhz 1vi0 1vi1 1vi2 1vi3 1vi4 1vi5 1vi6 1vi8 1vi9 1via 1vic 1vim 1viq 1vis 1viu 1viv 1vix 1viy 1viz

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.